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Updated: Aug 12, 2026

A Protocol for the Production of KLRG1 Tetramer
Published on: January 12, 2010
In vitro synthesis of L-gulono-gamma-lactone oxidase by rabbit reticulocyte lysate
T Koshizaka1, M Nishikimi, M Tanaka
1Institute of Applied Biochemistry, Yagi Memorial Park, Gifu, Japan.
Abstract:
In vitro synthesis of L-gulono-gamma-lactone oxidase [L-gulono-gamma-lactone:oxygen 2-oxidoreductase, EC 1.1.3.8], one of the microsomal flavin enzymes, was performed with poly(A)+ RNA of rat liver using the rabbit reticulocyte lysate system in order to study the biosynthesis of the enzyme. The apparent molecular weight of the synthesized enzyme protein was almost the same as that of the purified L-gulono-gamma-lactone oxidase from rat liver. It was demonstrated that the enzyme protein was not detectable when guinea pig poly(A)+ RNA was used for the translation, indicating that the mRNA for the enzyme is absent in the guinea pig or, if it exists, is not translatable.

